Saliva contains glycoproteins which are thought to in part mediate its protective functions for hard and soft oral tissues. All glycoproteins found in saliva from the parotid glands, have their oligosaccharides attached to asparagine residues; so-called N-linked glycoproteins. To study the mechanisms involved in processing, synthesis and secretion of N-linked secretory glycoproteins, we have utilized in vitro cell preparation from the rat parotid gland. We have examined (1) how an increase in N-linked protein glycosylation would influence glycoprotein secretion; (2) we have investigated the role of Beta-adrenergic receptors in the regulation of N-linked protein glycosylation; (3) since in the parotid gland, the Beta-adrenoreceptor is linked to the adenylate cyclase system the possibility of a generalized cyclic-AMP dependent regulatory step(s) in N-linked protein glycosylation has also been tested. In addition, we have characterized a Beta-adrenoreceptor antagonist, Bromoacetylal-prenololmenthane which irreversibly binds to Beta-receptors.